Cat: PA1000-9272

Recombinant Human NPFF Protein,His

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Analytical Data

  • Gene name

    NPFF

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    NPFF;Pro-FMRFamide-related neuropeptide FF

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    O15130

  • Expression Region

    66-76aa

  • AA Sequence

    SQAFLFQPQRF

  • Molecular Weight

    32.8 kDa

  • Endotoxin

    < 1.0 EU per μg protein as determined by the LAL method.

  • Form

    Freeze-dried powder

  • Buffer formulation

    PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

  • Reconstitution

    Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.

  • Customization

    Site-directed mutagenesis Custom tag design Custom buffer formulation Custom full-length protein production

  • Stability Test

    The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.

  • Storage & Shelf Life

    Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

  • Shipping

    In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.

Quality inspection process

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Protein Description

Neuropeptide FF (NPFF) is a neuropeptide that plays a significant role in various physiological processes, including pain modulation, stress response, and the regulation of reproductive functions. Initially discovered for its opioid-modulating effects, NPFF has garnered attention due to its diverse biological activities mediated through its interaction with NPFF receptors. The study of recombinant NPFF proteins has advanced our understanding of their structure, function, and potential therapeutic applications. Researchers have focused on characterizing NPFF's role in neurobiology and its implications in conditions such as chronic pain, anxiety, and depression. The ability to produce NPFF in recombinant systems allows for detailed investigations into its mechanisms of action, receptor interactions, and effects on neural circuits. Furthermore, recombinant NPFF proteins offer opportunities for the development of novel pharmacological agents that can target NPFF pathways, potentially leading to new treatments for pain management and other neuropsychological disorders. As research continues to uncover the complexities of NPFF signaling, the therapeutic potential of recombinant NPFF proteins remains a promising area of exploration within biomedical research.

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